ID A0A0G2FVX7_9PEZI Unreviewed; 1012 AA.
AC A0A0G2FVX7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative peroxide stress-activated histidine kinase mak1 {ECO:0000313|EMBL:KKY38079.1};
GN ORFNames=UCDDA912_g01836 {ECO:0000313|EMBL:KKY38079.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY38079.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY38079.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY38079.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY38079.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY38079.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY38079.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCUC01000061; KKY38079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FVX7; -.
DR STRING; 1214573.A0A0G2FVX7; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF74; HISTIDINE KINASE D5; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KKY38079.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Transferase {ECO:0000313|EMBL:KKY38079.1}.
FT DOMAIN 144..199
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 294..346
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 357..582
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 890..1012
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 205..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 942
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1012 AA; 112205 MW; 8ED17178C2D74C3B CRC64;
MPTNPSEMAL PTDKLKDLIL DSIPAQLFVT LPRTGEIVWV NSRYLAYRGQ SLAELHADPH
ASFHPDDRET YLKAWGRAVK TSTDFQMNVR IRRFDGAFRC FSARVVACKN KRNEIVYHLG
SYTDIHEQTM AELKVVRQQE IEASEAKYRF LANLIPQIIF TATEDEGITF ANEQWLAYTG
QSEGDALGLG FMDYVHPDDL AKCRIPSGHH SATPPLGRAR MSKRSQGEGH KANKPSEHPT
PNVESNIRGV HHPLSRQNSS SSDSVYELPS ANLTELAKDG VVKVGTDSNG RLSYSTEIRL
RTKTGEYRWH LVRCVEIDNI GNGGSSYFGS ATDINDHKLL EAKLKEAMES KSRFLSNMSH
EIRTPLIGIS GMVSFLQDTT LNEEQRDYTN TIQTSANSLL MIINDILDLS KVDAGMMKLN
HEWFHTRALI EDVNELVSAM AIARRLELNY IVEEDVPTWV KGDRVRIRQV LLNVIGNAIK
FTDTGEVFSR CRVRTDATGL GEQQVMLEFA VIDTGRGFTE EESKLIFKPF SQIDGSSTRA
HGGSGLGLVI SRQLVELHGG KMDGTAVPGW GATFTFTAKF SLPTADDHPD VPASPELPKT
PAVLEDIPTQ PFRQFTITKH RPSSAASPNH AEQQSSPAVA SSGSSNPSVT STGTRVTGRS
SISSVNVGLA RFSEAARASG QDLTQMKLEM PSGRTSPGQT PTPENPGKIV AAKEFRPPMF
SILVICPQKY SREATTQHIE MTLPKDVPHQ ITALASAQEA KQLISRDDPV IFTHILINLA
SSEEVLALIN EISSSTLLTK TKVVLLSDSI QRQALTKLVE DRNLADVISD SRVTYVYKPV
KPSRLAVVFD PAKEGDMSVD RNRSTAQQIV ETQKKSYREV EKRMGNKGYK VLLVEDNPVN
QKVLKKYLIK VGLEVELAAD GEECTSKVFG HDHGFYSLIL CDLHMPRKDG YQACREIRVW
EAKNKHGRMP IIALSANVMS DVQEKCVEAG FSDYVTKPVD FIDLSTALSK FF
//
